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Database: PDB
Entry: 3K2L
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HEADER    TRANSFERASE                             30-SEP-09   3K2L              
TITLE     CRYSTAL STRUCTURE OF DUAL-SPECIFICITY TYROSINE PHOSPHORYLATION        
TITLE    2 REGULATED KINASE 2 (DYRK2)                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DUAL SPECIFICITY TYROSINE-PHOSPHORYLATION-REGULATED KINASE 
COMPND   3 2;                                                                   
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: UNP RESIDUES 146-552;                                      
COMPND   6 SYNONYM: DYRK2;                                                      
COMPND   7 EC: 2.7.12.1;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: DYRK2;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-R3;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4                               
KEYWDS    DYRK2, DUAL-SPECIFICITY TYROSINE-(Y)-PHOSPHORYLATION REGULATED KINASE 
KEYWDS   2 2, PSK-H2, KINASE, STRUCTURAL GENOMICS CONSORTIUM, SGC, APOPTOSIS,   
KEYWDS   3 ATP-BINDING, MAGNESIUM, MANGANESE, NUCLEOTIDE-BINDING, NUCLEUS,      
KEYWDS   4 PHOSPHOPROTEIN, SERINE/THREONINE-PROTEIN KINASE, TRANSFERASE,        
KEYWDS   5 TYROSINE-PROTEIN KINASE                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.FILIPPAKOPOULOS,V.MYRIANTHOPOULOS,M.SOUNDARARAJAN,T.KROJER,E.HAPKA, 
AUTHOR   2 O.FEDOROV,G.BERRIDGE,J.WANG,L.SHRESTHA,A.C.W.PIKE,E.UGOCHUKWU,F.VON  
AUTHOR   3 DELFT,C.H.ARROWSMITH,A.EDWARDS,J.WEIGELT,C.BOUNTRA,E.MIKROS,S.KNAPP, 
AUTHOR   4 STRUCTURAL GENOMICS CONSORTIUM (SGC)                                 
REVDAT   3   26-JUN-13 3K2L    1       JRNL                                     
REVDAT   2   13-JUL-11 3K2L    1       VERSN                                    
REVDAT   1   13-OCT-09 3K2L    0                                                
JRNL        AUTH   M.SOUNDARARAJAN,A.K.ROOS,P.SAVITSKY,P.FILIPPAKOPOULOS,       
JRNL        AUTH 2 A.N.KETTENBACH,J.V.OLSEN,S.A.GERBER,J.ESWARAN,S.KNAPP,       
JRNL        AUTH 3 J.M.ELKINS                                                   
JRNL        TITL   STRUCTURES OF DOWN SYNDROME KINASES, DYRKS, REVEAL           
JRNL        TITL 2 MECHANISMS OF KINASE ACTIVATION AND SUBSTRATE RECOGNITION.   
JRNL        REF    STRUCTURE                     V.  21   986 2013              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   23665168                                                     
JRNL        DOI    10.1016/J.STR.2013.03.012                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.36 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0089                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.36                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.54                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 22694                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.228                           
REMARK   3   R VALUE            (WORKING SET) : 0.225                           
REMARK   3   FREE R VALUE                     : 0.288                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1160                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.36                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.42                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1564                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.88                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4260                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 76                           
REMARK   3   BIN FREE R VALUE                    : 0.5540                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3143                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 13                                      
REMARK   3   SOLVENT ATOMS            : 58                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 63.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.01                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.53000                                              
REMARK   3    B22 (A**2) : 1.53000                                              
REMARK   3    B33 (A**2) : -3.05000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.331         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.268         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.218         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.305        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.943                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.907                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3241 ; 0.014 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  2161 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4405 ; 1.602 ; 1.975       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5251 ; 0.915 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   404 ; 6.918 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   145 ;34.874 ;23.448       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   514 ;16.034 ;15.088       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    21 ;20.908 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   476 ; 0.092 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3611 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   666 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2025 ; 4.196 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   822 ; 1.248 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3226 ; 6.116 ; 5.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1216 ;10.724 ; 8.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1179 ;12.453 ;11.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    62        A   230                          
REMARK   3    ORIGIN FOR THE GROUP (A):  48.0258  28.3075  23.9966              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2636 T22:   0.0724                                     
REMARK   3      T33:   0.1156 T12:  -0.0404                                     
REMARK   3      T13:  -0.0727 T23:   0.0054                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.1617 L22:   1.5067                                     
REMARK   3      L33:   2.6309 L12:  -0.0996                                     
REMARK   3      L13:   1.1521 L23:   0.1549                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1766 S12:   0.5143 S13:  -0.0670                       
REMARK   3      S21:  -0.3973 S22:  -0.0071 S23:  -0.0172                       
REMARK   3      S31:  -0.4128 S32:   0.3443 S33:   0.1837                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   231        A   470                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.0262  28.9314  12.9850              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0842 T22:   0.1529                                     
REMARK   3      T33:   0.0824 T12:   0.0885                                     
REMARK   3      T13:  -0.0537 T23:  -0.0250                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1105 L22:   1.8823                                     
REMARK   3      L33:   5.7325 L12:  -0.1791                                     
REMARK   3      L13:   1.6526 L23:   0.0005                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2698 S12:  -0.0441 S13:   0.2816                       
REMARK   3      S21:  -0.0622 S22:   0.0205 S23:   0.2726                       
REMARK   3      S31:  -0.4299 S32:  -0.7363 S33:   0.2493                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES: RESIDUAL ONLY                                   
REMARK   4                                                                      
REMARK   4 3K2L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-OCT-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB055466.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-JUN-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9763                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22801                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.360                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.190                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 6.200                              
REMARK 200  R MERGE                    (I) : 0.08200                            
REMARK 200  R SYM                      (I) : 0.08200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.36                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.89900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.89900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2VX3                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.59                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.26M (NH4)2SO4, 0.20M LI2SO4, 0.1M      
REMARK 280  TRIS PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       42.14250            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       42.14250            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       74.25250            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       42.14250            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       42.14250            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       74.25250            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       42.14250            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       42.14250            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       74.25250            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       42.14250            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       42.14250            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       74.25250            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    50                                                      
REMARK 465     HIS A    51                                                      
REMARK 465     HIS A    52                                                      
REMARK 465     HIS A    53                                                      
REMARK 465     HIS A    54                                                      
REMARK 465     HIS A    55                                                      
REMARK 465     HIS A    56                                                      
REMARK 465     SER A    57                                                      
REMARK 465     SER A    58                                                      
REMARK 465     GLY A    59                                                      
REMARK 465     GLN A    71                                                      
REMARK 465     SER A    72                                                      
REMARK 465     GLY A   123                                                      
REMARK 465     THR A   471                                                      
REMARK 465     GLY A   472                                                      
REMARK 465     GLU A   473                                                      
REMARK 465     LYS A   474                                                      
REMARK 465     THR A   475                                                      
REMARK 465     SER A   476                                                      
REMARK 465     VAL A   477                                                      
REMARK 465     LYS A   478                                                      
REMARK 465     ARG A   479                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     VAL A  60    CG1  CG2                                            
REMARK 470     MET A  73    CG   SD   CE                                        
REMARK 470     LYS A  77    CE   NZ                                             
REMARK 470     LYS A  88    CG   CD   CE   NZ                                   
REMARK 470     GLN A  92    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  93    CG   CD   CE   NZ                                   
REMARK 470     LYS A 116    CD   CE   NZ                                        
REMARK 470     LYS A 117    CG   CD   CE   NZ                                   
REMARK 470     ARG A 118    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 134    CD   OE1  NE2                                       
REMARK 470     SER A 136    OG                                                  
REMARK 470     GLN A 139    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 153    CG   CD   CE   NZ                                   
REMARK 470     LYS A 157    CG   CD   CE   NZ                                   
REMARK 470     PHE A 160    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN A 162    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 181    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A 182    CG   OD1  ND2                                       
REMARK 470     GLU A 183    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 184    CG   CD   CE   NZ                                   
REMARK 470     ARG A 185    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 188    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 189    CD   OE1  NE2                                       
REMARK 470     ARG A 195    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 198    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 205    CG   CD   CE   NZ                                   
REMARK 470     ASN A 222    CG   OD1  ND2                                       
REMARK 470     LYS A 241    CD   CE   NZ                                        
REMARK 470     LYS A 243    CE   NZ                                             
REMARK 470     LYS A 268    CG   CD   CE   NZ                                   
REMARK 470     GLN A 286    CD   OE1  NE2                                       
REMARK 470     GLN A 304    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 377    CD   CE   NZ                                        
REMARK 470     LYS A 380    CG   CD   CE   NZ                                   
REMARK 470     VAL A 383    CG1  CG2                                            
REMARK 470     LYS A 386    CG   CD   CE   NZ                                   
REMARK 470     TYR A 388    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     SER A 398    OG                                                  
REMARK 470     LYS A 428    CD   CE   NZ                                        
REMARK 470     ARG A 463    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG A 464    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 465    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 468    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A 148      -49.75   -140.57                                   
REMARK 500    LEU A 231     -163.25   -108.48                                   
REMARK 500    SER A 232     -152.15   -109.99                                   
REMARK 500    CYS A 274       -1.73     75.91                                   
REMARK 500    ASP A 275       39.82   -147.15                                   
REMARK 500    ASP A 295       89.71     61.29                                   
REMARK 500    GLU A 302      -37.66    -37.52                                   
REMARK 500    TPO A 308      -51.50   -130.27                                   
REMARK 500    GLN A 311      164.94     66.37                                   
REMARK 500    ALA A 375       21.82    -72.97                                   
REMARK 500    PRO A 469       -8.53    -51.03                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A  42        DISTANCE =  7.03 ANGSTROMS                       
REMARK 525    HOH A 495        DISTANCE =  5.42 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 480  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A 285   N                                                      
REMARK 620 2 ARG A 288   O   124.3                                              
REMARK 620 3 GLY A 290   O   113.8 104.0                                        
REMARK 620 4 GLN A 285   O    54.6  71.0 145.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 480                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 481                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 482                  
DBREF  3K2L A   73   479  UNP    Q92630   DYRK2_HUMAN    146    552             
SEQADV 3K2L MET A   50  UNP  Q92630              INITIATING METHIONINE          
SEQADV 3K2L HIS A   51  UNP  Q92630              EXPRESSION TAG                 
SEQADV 3K2L HIS A   52  UNP  Q92630              EXPRESSION TAG                 
SEQADV 3K2L HIS A   53  UNP  Q92630              EXPRESSION TAG                 
SEQADV 3K2L HIS A   54  UNP  Q92630              EXPRESSION TAG                 
SEQADV 3K2L HIS A   55  UNP  Q92630              EXPRESSION TAG                 
SEQADV 3K2L HIS A   56  UNP  Q92630              EXPRESSION TAG                 
SEQADV 3K2L SER A   57  UNP  Q92630              EXPRESSION TAG                 
SEQADV 3K2L SER A   58  UNP  Q92630              EXPRESSION TAG                 
SEQADV 3K2L GLY A   59  UNP  Q92630              EXPRESSION TAG                 
SEQADV 3K2L VAL A   60  UNP  Q92630              EXPRESSION TAG                 
SEQADV 3K2L ASP A   61  UNP  Q92630              EXPRESSION TAG                 
SEQADV 3K2L LEU A   62  UNP  Q92630              EXPRESSION TAG                 
SEQADV 3K2L GLY A   63  UNP  Q92630              EXPRESSION TAG                 
SEQADV 3K2L THR A   64  UNP  Q92630              EXPRESSION TAG                 
SEQADV 3K2L GLU A   65  UNP  Q92630              EXPRESSION TAG                 
SEQADV 3K2L ASN A   66  UNP  Q92630              EXPRESSION TAG                 
SEQADV 3K2L LEU A   67  UNP  Q92630              EXPRESSION TAG                 
SEQADV 3K2L TYR A   68  UNP  Q92630              EXPRESSION TAG                 
SEQADV 3K2L PHE A   69  UNP  Q92630              EXPRESSION TAG                 
SEQADV 3K2L GLN A   71  UNP  Q92630              EXPRESSION TAG                 
SEQADV 3K2L SER A   72  UNP  Q92630              EXPRESSION TAG                 
SEQRES   1 A  429  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  429  GLY THR GLU ASN LEU TYR PHE GLN SER MET GLY LYS VAL          
SEQRES   3 A  429  LYS ALA THR PRO MET THR PRO GLU GLN ALA MET LYS GLN          
SEQRES   4 A  429  TYR MET GLN LYS LEU THR ALA PHE GLU HIS HIS GLU ILE          
SEQRES   5 A  429  PHE SER TYR PRO GLU ILE TYR PHE LEU GLY LEU ASN ALA          
SEQRES   6 A  429  LYS LYS ARG GLN GLY MET THR GLY GLY PRO ASN ASN GLY          
SEQRES   7 A  429  GLY TYR ASP ASP ASP GLN GLY SER TYR VAL GLN VAL PRO          
SEQRES   8 A  429  HIS ASP HIS VAL ALA TYR ARG TYR GLU VAL LEU LYS VAL          
SEQRES   9 A  429  ILE GLY LYS GLY SEP PHE GLY GLN VAL VAL LYS ALA TYR          
SEQRES  10 A  429  ASP HIS LYS VAL HIS GLN HIS VAL ALA LEU LYS MET VAL          
SEQRES  11 A  429  ARG ASN GLU LYS ARG PHE HIS ARG GLN ALA ALA GLU GLU          
SEQRES  12 A  429  ILE ARG ILE LEU GLU HIS LEU ARG LYS GLN ASP LYS ASP          
SEQRES  13 A  429  ASN THR MET ASN VAL ILE HIS MET LEU GLU ASN PHE THR          
SEQRES  14 A  429  PHE ARG ASN HIS ILE CYS MET THR PHE GLU LEU LEU SER          
SEQRES  15 A  429  MET ASN LEU TYR GLU LEU ILE LYS LYS ASN LYS PHE GLN          
SEQRES  16 A  429  GLY PHE SER LEU PRO LEU VAL ARG LYS PHE ALA HIS SER          
SEQRES  17 A  429  ILE LEU GLN CYS LEU ASP ALA LEU HIS LYS ASN ARG ILE          
SEQRES  18 A  429  ILE HIS CYS ASP LEU LYS PRO GLU ASN ILE LEU LEU LYS          
SEQRES  19 A  429  GLN GLN GLY ARG SER GLY ILE LYS VAL ILE ASP PHE GLY          
SEQRES  20 A  429  SER SER CYS TYR GLU HIS GLN ARG VAL TYR TPO PTR ILE          
SEQRES  21 A  429  GLN SER ARG PHE TYR ARG ALA PRO GLU VAL ILE LEU GLY          
SEQRES  22 A  429  ALA ARG TYR GLY MET PRO ILE ASP MET TRP SER LEU GLY          
SEQRES  23 A  429  CYS ILE LEU ALA GLU LEU LEU THR GLY TYR PRO LEU LEU          
SEQRES  24 A  429  PRO GLY GLU ASP GLU GLY ASP GLN LEU ALA CYS MET ILE          
SEQRES  25 A  429  GLU LEU LEU GLY MET PRO SEP GLN LYS LEU LEU ASP ALA          
SEQRES  26 A  429  SER LYS ARG ALA LYS ASN PHE VAL SER SEP LYS GLY TYR          
SEQRES  27 A  429  PRO ARG TYR CYS THR VAL THR THR LEU SER ASP GLY SER          
SEQRES  28 A  429  VAL VAL LEU ASN GLY GLY ARG SER ARG ARG GLY LYS LEU          
SEQRES  29 A  429  ARG GLY PRO PRO GLU SER ARG GLU TRP GLY ASN ALA LEU          
SEQRES  30 A  429  LYS GLY CYS ASP ASP PRO LEU PHE LEU ASP PHE LEU LYS          
SEQRES  31 A  429  GLN CYS LEU GLU TRP ASP PRO ALA VAL ARG MET THR PRO          
SEQRES  32 A  429  GLY GLN ALA LEU ARG HIS PRO TRP LEU ARG ARG ARG LEU          
SEQRES  33 A  429  PRO LYS PRO PRO THR GLY GLU LYS THR SER VAL LYS ARG          
MODRES 3K2L SEP A  159  SER  PHOSPHOSERINE                                      
MODRES 3K2L TPO A  308  THR  PHOSPHOTHREONINE                                   
MODRES 3K2L PTR A  309  TYR  O-PHOSPHOTYROSINE                                  
MODRES 3K2L SEP A  369  SER  PHOSPHOSERINE                                      
MODRES 3K2L SEP A  385  SER  PHOSPHOSERINE                                      
HET    SEP  A 159      10                                                       
HET    TPO  A 308      11                                                       
HET    PTR  A 309      16                                                       
HET    SEP  A 369      10                                                       
HET    SEP  A 385      10                                                       
HET    SO4  A   1       5                                                       
HET    SO4  A   2       5                                                       
HET     NA  A 480       1                                                       
HET     CL  A 481       1                                                       
HET     CL  A 482       1                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETNAM     SO4 SULFATE ION                                                      
HETNAM      NA SODIUM ION                                                       
HETNAM      CL CHLORIDE ION                                                     
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     PTR PHOSPHONOTYROSINE                                                
FORMUL   1  SEP    3(C3 H8 N O6 P)                                              
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   1  PTR    C9 H12 N O6 P                                                
FORMUL   2  SO4    2(O4 S 2-)                                                   
FORMUL   4   NA    NA 1+                                                        
FORMUL   5   CL    2(CL 1-)                                                     
FORMUL   7  HOH   *58(H2 O)                                                     
HELIX    1   1 ASP A   61  GLU A   65  5                                   5    
HELIX    2   2 THR A   82  MET A   91  1                                  10    
HELIX    3   3 GLN A   92  LEU A   94  5                                   3    
HELIX    4   4 PHE A   97  ILE A  102  1                                   6    
HELIX    5   5 PHE A  103  TYR A  105  5                                   3    
HELIX    6   6 GLY A  124  TYR A  130  1                                   7    
HELIX    7   7 GLU A  183  LYS A  202  1                                  20    
HELIX    8   8 ASN A  234  ASN A  242  1                                   9    
HELIX    9   9 SER A  248  ASN A  269  1                                  22    
HELIX   10  10 LYS A  277  GLU A  279  5                                   3    
HELIX   11  11 HIS A  303  ARG A  305  5                                   3    
HELIX   12  12 SER A  312  ARG A  316  5                                   5    
HELIX   13  13 ALA A  317  GLY A  323  1                                   7    
HELIX   14  14 MET A  328  GLY A  345  1                                  18    
HELIX   15  15 ASP A  353  GLY A  366  1                                  14    
HELIX   16  16 SEP A  369  ALA A  375  1                                   7    
HELIX   17  17 ARG A  378  VAL A  383  1                                   6    
HELIX   18  18 GLU A  422  LEU A  427  1                                   6    
HELIX   19  19 ASP A  432  LEU A  443  1                                  12    
HELIX   20  20 THR A  452  ARG A  458  1                                   7    
SHEET    1   A 2 ASN A  66  TYR A  68  0                                        
SHEET    2   A 2 LYS A  77  THR A  79 -1  O  LYS A  77   N  TYR A  68           
SHEET    1   B 6 HIS A 144  VAL A 145  0                                        
SHEET    2   B 6 TYR A 149  LYS A 157 -1  O  TYR A 149   N  VAL A 145           
SHEET    3   B 6 GLY A 161  ASP A 168 -1  O  TYR A 167   N  GLU A 150           
SHEET    4   B 6 GLN A 173  VAL A 180 -1  O  MET A 179   N  GLN A 162           
SHEET    5   B 6 HIS A 223  PHE A 228 -1  O  MET A 226   N  LYS A 178           
SHEET    6   B 6 MET A 214  PHE A 220 -1  N  LEU A 215   O  THR A 227           
SHEET    1   C 2 ILE A 271  ILE A 272  0                                        
SHEET    2   C 2 CYS A 300  TYR A 301 -1  O  CYS A 300   N  ILE A 272           
SHEET    1   D 2 ILE A 281  LEU A 283  0                                        
SHEET    2   D 2 ILE A 291  VAL A 293 -1  O  LYS A 292   N  LEU A 282           
SHEET    1   E 2 VAL A 394  THR A 396  0                                        
SHEET    2   E 2 VAL A 402  LEU A 404 -1  O  VAL A 403   N  THR A 395           
SHEET    1   F 2 GLY A 407  ARG A 408  0                                        
SHEET    2   F 2 LEU A 414  ARG A 415 -1  O  ARG A 415   N  GLY A 407           
LINK         C   GLY A 158                 N   SEP A 159     1555   1555  1.33  
LINK         C   SEP A 159                 N   PHE A 160     1555   1555  1.34  
LINK         C   TYR A 307                 N   TPO A 308     1555   1555  1.33  
LINK         C   TPO A 308                 N   PTR A 309     1555   1555  1.33  
LINK         C   PTR A 309                 N   ILE A 310     1555   1555  1.35  
LINK         C   PRO A 368                 N   SEP A 369     1555   1555  1.34  
LINK         C   SEP A 369                 N   GLN A 370     1555   1555  1.33  
LINK         C   SER A 384                 N   SEP A 385     1555   1555  1.32  
LINK         C   SEP A 385                 N   LYS A 386     1555   1555  1.34  
LINK         N   GLN A 285                NA    NA A 480     1555   1555  2.90  
LINK         O   ARG A 288                NA    NA A 480     1555   1555  2.69  
LINK         O   GLY A 290                NA    NA A 480     1555   1555  2.49  
LINK         O   GLN A 285                NA    NA A 480     1555   1555  3.01  
CISPEP   1 SER A  398    ASP A  399          0        10.99                     
CISPEP   2 ASP A  399    GLY A  400          0         1.90                     
CISPEP   3 GLY A  400    SER A  401          0       -15.07                     
SITE     1 AC1  2 ARG A 378  ASN A 381                                          
SITE     1 AC2  3 ARG A 421  ASN A 425  ALA A 426                               
SITE     1 AC3  4 LYS A 284  GLN A 285  ARG A 288  GLY A 290                    
SITE     1 AC4  1 HIS A 174                                                     
SITE     1 AC5  2 ARG A 411  LYS A 413                                          
CRYST1   84.285   84.285  148.505  90.00  90.00  90.00 P 42 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011865  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011865  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006734        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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